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Tissue injury and repair
Published in C. Simon Herrington, Muir's Textbook of Pathology, 2020
The extracellular matrix contains several large glycoproteins, which act as adhesion molecules that link matrix components to each other and to surrounding cells. The most abundant of these is fibronectin. This protein binds to other matrix components such as collagens via specific peptide domains on its molecule and to cells via a three amino acid sequence (arginine–glycine–aspartic acid; RGD). Laminin is the principal structural glycoprotein of basement membranes. This also has cell- and matrix-binding domains. It has the capacity to alter the morphology and differentiation of a wide range of cell types. Another group of related proteins – matricellular proteins – do not function as structural proteins, but rather have regulatory roles. These may be important during tissue remodelling and include osteonectin and tenascin.
Angiogenesis and Roles of Adhesion Molecules in Psoriatic Disease
Published in Siba P. Raychaudhuri, Smriti K. Raychaudhuri, Debasis Bagchi, Psoriasis and Psoriatic Arthritis, 2017
Asmita Hazra, Saptarshi Mandal
It plays diverse roles in platelet aggregation, angiogenesis, and tumorigenesis. TSP1 and 2 are secreted into the ECM, but rather than serving structural roles, they have regulatory influence on cellular behavior by interaction with numerous receptors, proteases, cytokines, and so forth, and are thus are termed “matricellular” proteins.
Management of idiopathic pulmonary fibrosis
Published in Muhunthan Thillai, David R Moller, Keith C Meyer, Clinical Handbook of Interstitial Lung Disease, 2017
Damian AD Bruce-Hickman, Helen Garthwaite, Melissa Heightman, Bibek Gooptu
Connective tissue growth factor (CTGF) is a matricellular protein that can play roles in epithelial–mesenchymal transition, activation of myofibroblasts, remodelling of extracellular matrix and stimulation of TGF-β release (160). In mouse models, inhibition of CTGF not only reduced, but could even reverse the fibrotic effects of radiation (161). FG-3019, an inhibitor of CTGF, has been trialed in human subjects with IPF in an open-label study (162). Twenty percent of patients experienced reduction in fibrotic load, as measured by CT scanning. Further placebo-controlled RCTs are required to confirm these findings, and, if successful, to identify and validate stratifying factors associated with differences in response (163).
Left Ventricular Reverse Remodeling in Heart Failure: Remission to Recovery
Published in Structural Heart, 2021
Jacinthe Boulet, Mandeep R. Mehra
Compared with healthy myocardium, both non-ischemic and ischemic dilated CMP may lead to a significant increase in myocardial MMP activity and reduction in expression and activity of tissue inhibitors of metalloproteinases (TIMP), leading to myocyte reorganization and collagen matrix breakdown.31,32 Modification of the extracellular matrix (ECM) secondary to altered MMP and TIMP gene expression may also influence intercellular communication through the ability of the ECM to influence extracellular cytokines and signaling proteins via the matricellular proteins. These include osteopontin, osteonectin, thrombospondins, tenascin, and periostin, which will interact with cell-surface receptors and growth factors, linking ECM proteins together and modulate cell behavior.33 The activity of matricellular proteins will be enhanced in response to cardiac injury or other neurohormonal stressors.33
Skin proteomics – analysis of the extracellular matrix in health and disease
Published in Expert Review of Proteomics, 2020
Jörn Dengjel, Leena Bruckner-Tuderman, Alexander Nyström
The matricellular protein SPARC (Secreted Protein, Acidic, Rich in Cysteine), also known as BM40 or osteonectin, has its highest abundance in the papillary dermis [90]. It interacts directly with collagen I, III, and V [91] and may regulate maturation of procollagens and fibrillogenesis in the skin [92]. Periostin, another matricellular protein in the papillary ECM [93] can regulate collagen fibrillogenesis by directly interacting with collagen I [94]. It also interacts with BMP-1 evoking proteolytic activation of lysyl oxidase and subsequent collagen crosslinking [95]. During homeostasis the abundance of matricellular proteins is generally low in skin; however, after tissue damage or under pathological conditions they can be greatly increased and also involved in driving pathological processes such as fibrosis. In addition to the aforementioned matricellular proteins, these also include thrombospondin-1 and tenascin-c [12].
Matricellular Proteins Play a Potential Role in Acute Primary Angle Closure
Published in Current Eye Research, 2018
Jing Wang, Mingshui Fu, Kun Liu, Ning Wang, Zhihua Zhang, Minwen Zhou, Xun Xu
The term “matricellular protein” was introduced in 1995 by Paul Bornstein, and refers to a group of nonstructural modular extracellular proteins. Their functions are to bind to matrix proteins or cell surface receptors, or interact indirectly with growth factors and proteases.5 Matricellular proteins include secreted proteins such as cysteine (SPARC), thrombospondin-1 and -2, tenascin-C, and osteopontin.6–10 Previous studies have shown that matricellular proteins are widely expressed in eyes with glaucoma including those with primary open-angle glaucoma, pseudo-exfoliative glaucoma, corticosteroid glaucoma, and autoimmune glaucoma,11–15 suggesting that these proteins play an important role in the pathogenesis of these diseases.